scholarly journals Crucial Role of H322 in Folding of the Diphtheria Toxin T-Domain into the Open-Channel State

Biochemistry ◽  
2013 ◽  
Vol 52 (20) ◽  
pp. 3457-3463 ◽  
Author(s):  
Mauricio Vargas-Uribe ◽  
Mykola V. Rodnin ◽  
Paul Kienker ◽  
Alan Finkelstein ◽  
Alexey S. Ladokhin
Keyword(s):  
Crucial Role ◽  
Diphtheria Toxin ◽  
Open Channel ◽  
Channel State ◽  
T Domain

scholarly journals Crucial Role of H322 in the Folding of Diphtheria Toxin T-Domain into the Open-Channel State

2014 ◽  
Vol 106 (2) ◽  
pp. 717a
Author(s):  
Mauricio Vargas-Uribe ◽  
Mykola V. Rodnin ◽  
Paul Kienker ◽  
Alan Finkelstein ◽  
Alexey S. Ladokhin
Keyword(s):  
Crucial Role ◽  
Diphtheria Toxin ◽  
Open Channel ◽  
Channel State ◽  
T Domain

scholarly journals Topography of Diphtheria Toxin's T Domain in the Open Channel State

2000 ◽  
Vol 115 (4) ◽  
pp. 421-434 ◽  
Author(s):  
Lisa Senzel ◽  
Michael Gordon ◽  
Robert O. Blaustein ◽  
K. Joon Oh ◽  
R. John Collier ◽  
...  
Keyword(s):  
Diphtheria Toxin ◽  
Open Channel ◽  
Catalytic Domain ◽  
Water Soluble ◽  
Soluble Form ◽  
Crystallographic Structure ◽  
Channel State ◽  
Amino Terminal ◽  
T Domain ◽  
Membrane Spanning

When diphtheria toxin encounters a low pH environment, the channel-forming T domain undergoes a poorly understood conformational change that allows for both its own membrane insertion and the translocation of the toxin's catalytic domain across the membrane. From the crystallographic structure of the water-soluble form of diphtheria toxin, a “double dagger” model was proposed in which two transmembrane helical hairpins, TH5-7 and TH8-9, anchor the T domain in the membrane. In this paper, we report the topography of the T domain in the open channel state. This topography was derived from experiments in which either a hexahistidine (H6) tag or biotin moiety was attached at residues that were mutated to cysteines. From the sign of the voltage gating induced by the H6 tag and the accessibility of the biotinylated residues to streptavidin added to the cis or trans side of the membrane, we determined which segments of the T domain are on the cis or trans side of the membrane and, consequently, which segments span the membrane. We find that there are three membrane-spanning segments. Two of them are in the channel-forming piece of the T domain, near its carboxy terminal end, and correspond to one of the proposed “daggers,” TH8-9. The other membrane-spanning segment roughly corresponds to only TH5 of the TH5-7 dagger, with the rest of that region lying on or near the cis surface. We also find that, in association with channel formation, the amino terminal third of the T domain, a hydrophilic stretch of ∼70 residues, is translocated across the membrane to the trans side.

scholarly journals Evidence for a TH6-TH7 Transmembrane Hairpin in the Diphtheria Toxin T-Domain Open Channel State

2012 ◽  
Vol 102 (3) ◽  
pp. 657a
Author(s):  
Paul Kienker ◽  
Zhengyan Wu ◽  
Alan Finkelstein
Keyword(s):  
Diphtheria Toxin ◽  
Open Channel ◽  
Channel State ◽  
T Domain

scholarly journals Cellular Entry of the Diphtheria Toxin Does Not Require the Formation of the Open-Channel State by Its Translocation Domain

Toxins ◽  
2017 ◽  
Vol 9 (10) ◽  
pp. 299 ◽  
Author(s):  
Alexey Ladokhin ◽  
Mauricio Vargas-Uribe ◽  
Mykola Rodnin ◽  
Chiranjib Ghatak ◽  
Onkar Sharma
Keyword(s):  
Diphtheria Toxin ◽  
Open Channel ◽  
Channel State ◽  
Translocation Domain ◽  
Cellular Entry

scholarly journals pH-Triggered Membrane Insertion Pathway of the Diphtheria Toxin T-Domain: 2. Role of Histidines

2009 ◽  
Vol 96 (3) ◽  
pp. 433a
Author(s):  
Mykola V. Rodnin ◽  
Alexander Kyrychenko ◽  
Yevgen O. Posokhov ◽  
Joshua Brettmann ◽  
Anna Thoma ◽  
...  
Keyword(s):  
Diphtheria Toxin ◽  
Membrane Insertion ◽  
T Domain

scholarly journals Role of Acidic Residues in Helices TH8–TH9 in Membrane Interactions of the Diphtheria Toxin T Domain

Toxins ◽  
2015 ◽  
Vol 7 (4) ◽  
pp. 1303-1323 ◽  
Author(s):  
Chiranjib Ghatak ◽  
Mykola Rodnin ◽  
Mauricio Vargas-Uribe ◽  
Andrew McCluskey ◽  
Jose Flores-Canales ◽  
...  
Keyword(s):  
Diphtheria Toxin ◽  
Membrane Interactions ◽  
Acidic Residues ◽  
T Domain

Epitaxial YBa2Cu3O7-8 films : Crucial role of growth-induced linear defects in microwave properties

2001 ◽  
Vol 11 (PR11) ◽  
pp. Pr11-47-Pr11-52
Author(s):  
V. M. Pan ◽  
V. S. Flis ◽  
V. A. Komashko ◽  
O. G. Plys ◽  
C. G. Tretiatchenko ◽  
...  
Keyword(s):  
Crucial Role ◽  
Microwave Properties ◽  
Linear Defects
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